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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
8
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pubmed:dateCreated |
1989-1-4
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pubmed:abstractText |
BHK cells transfected with human lysosomal acid phosphatase (LAP) cDNA (CT29) expressed 70-fold higher enzyme activities of acid phosphatase than non-transfected BHK cells. The CT29-LAP was synthesized in BHK cells as a heterogeneously glycosylated precursor that was tightly membrane associated. Transfer to the trans-Golgi was associated with a small increase in size (approximately 7 kd) and partial processing of the oligosaccharides to complex type structures. CT29-LAP was transferred into lysosomes as shown by subcellular fractionation, immunofluorescence and immunoelectron microscopy. Lack of mannose-6-phosphate residues suggested that transport does not involve mannose-6-phosphate receptors. Part of the membrane-associated CT29-LAP was processed to a soluble form. The mechanism that converts CT29-LAP into a soluble form was sensitive to NH4Cl, and reduced the size of the polypeptide by 7 kd. In vitro translation of CT29-derived cRNA in the presence of microsomal membranes yielded a CT29-LAP precursor that is protected from proteinase K except for a small peptide of approximately 2 kd. In combination with the sequence data available for LAP, these observations suggest that CT29-LAP is synthesized and transported to lysosomes as a transmembrane protein. In the lysosomes, CT29-LAP is released from the membrane by proteolytic cleavage, which removes a C-terminal peptide including the transmembrane domain and the cytosolic tail of 18 amino acids.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/3056714-194704,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3056714-2409098,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3056714-2871029,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3056714-2943218,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3056714-2959299,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3056714-2960521,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3056714-3003148,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3056714-3034252,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3056714-3160696,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3056714-3191910,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3056714-3339090,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3056714-3714487,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3056714-3782140,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3056714-3896128,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3056714-3904632,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3056714-3922993,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3056714-4015620,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3056714-4850204,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3056714-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3056714-6122572,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3056714-6136972,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3056714-6155266,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3056714-6236213,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3056714-6417138,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3056714-6989822,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3056714-825524
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0261-4189
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
7
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2351-8
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:3056714-Acid Phosphatase,
pubmed-meshheading:3056714-Animals,
pubmed-meshheading:3056714-Biological Transport,
pubmed-meshheading:3056714-Cell Fractionation,
pubmed-meshheading:3056714-Cell Line,
pubmed-meshheading:3056714-Cell Membrane,
pubmed-meshheading:3056714-Centrifugation, Density Gradient,
pubmed-meshheading:3056714-DNA,
pubmed-meshheading:3056714-Fluorescent Antibody Technique,
pubmed-meshheading:3056714-Gene Expression Regulation,
pubmed-meshheading:3056714-Humans,
pubmed-meshheading:3056714-Immunohistochemistry,
pubmed-meshheading:3056714-Lysosomes,
pubmed-meshheading:3056714-Membrane Proteins,
pubmed-meshheading:3056714-Phosphorylation,
pubmed-meshheading:3056714-Precipitin Tests,
pubmed-meshheading:3056714-Protein Biosynthesis,
pubmed-meshheading:3056714-Protein Precursors,
pubmed-meshheading:3056714-Transcription, Genetic,
pubmed-meshheading:3056714-Transfection
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pubmed:year |
1988
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pubmed:articleTitle |
Human lysosomal acid phosphatase is transported as a transmembrane protein to lysosomes in transfected baby hamster kidney cells.
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pubmed:affiliation |
Zentrum Biochemie, Universität Göttingen, FRG.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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